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Willy J. Peumans - One of the best experts on this subject based on the ideXlab platform.
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Analysis of the sugar‐binding specificity of mannose‐binding‐type Jacalin‐related lectins by frontal affinity chromatography – an approach to functional classification
FEBS Journal, 2008Co-Authors: Sachiko Nakamura-tsuruta, Willy J. Peumans, E J Van Damme, Noboru Uchiyama, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:The Jacalin-related lectin (JRL) family comprises galactose-binding-type (gJRLs) and mannose-binding-type (mJRLs) lectins. Although the documented occurrence of gJRLs is confined to the family Moraceae, mJRLs are widespread in the plant kingdom. A detailed comparison of sugar-binding specificity was made by frontal affinity chromatography to corroborate the structure-function relationships of the extended mJRL subfamily. Eight mJRLs covering a broad taxonomic range were used: Artocarpin from Artocarpus integrifolia (jackfruit, Moraceae), BanLec from Musa acuminata (banana, Musaceae), Calsepa from Calystegia sepium (hedge bindweed, Convolvulaceae), CCA from Castanea crenata (Japanese chestnut, Fagaceae), Conarva from Convolvulus arvensis (bindweed, Convolvulaceae), CRLL from Cycas revoluta (King Sago palm tree, Cycadaceae), Heltuba from Helianthus tuberosus (Jerusalem artichoke, Asteraceae) and MornigaM from Morus nigra (black mulberry, Moraceae). The result using 103 pyridylaminated glycans clearly divided the mJRLs into two major groups, each of which was further divided into two subgroups based on the preference for high-mannose-type N-glycans. This criterion also applied to the binding preference for complex-type N-glycans. Notably, the result of cluster analysis of the amino acid sequences clearly corresponded to the above specificity classification. Thus, marked correlation between the sugar-binding specificity of mJRLs and their phylogeny should shed light on the functional significance of JRLs.
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The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold
Journal of Biological Chemistry, 2003Co-Authors: Yves Bourne, Willy J. Peumans, Annick Barre, E J Van Damme, Véronique Roig-zamboni, Corinne Houlès Astoul, Pierre RougéAbstract:Abstract The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same β-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded β-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the β-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
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Structure of an RNase-related protein from Calystegia sepium.
Acta Crystallographica Section D Biological Crystallography, 2002Co-Authors: Anja Rabijns, Willy J. Peumans, Christel Verboven, Pierre Rougé, Annick Barre, E. J. M. Van Damme, C. J. De RanterAbstract:The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical α + β structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the `active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
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Structure of an RNase-related protein from Calystegia sepium.
Acta crystallographica. Section D Biological crystallography, 2002Co-Authors: Anja Rabijns, Willy J. Peumans, Christel Verboven, Pierre Rougé, Annick Barre, E. J. M. Van Damme, C. J. De RanterAbstract:The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
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Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β‐amylase from Calystegia sepium (hedge bindweed) rhizomes
European Journal of Biochemistry, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
E J Van Damme - One of the best experts on this subject based on the ideXlab platform.
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Analysis of the sugar‐binding specificity of mannose‐binding‐type Jacalin‐related lectins by frontal affinity chromatography – an approach to functional classification
FEBS Journal, 2008Co-Authors: Sachiko Nakamura-tsuruta, Willy J. Peumans, E J Van Damme, Noboru Uchiyama, Kiichiro Totani, Yukishige Ito, Jun HirabayashiAbstract:The Jacalin-related lectin (JRL) family comprises galactose-binding-type (gJRLs) and mannose-binding-type (mJRLs) lectins. Although the documented occurrence of gJRLs is confined to the family Moraceae, mJRLs are widespread in the plant kingdom. A detailed comparison of sugar-binding specificity was made by frontal affinity chromatography to corroborate the structure-function relationships of the extended mJRL subfamily. Eight mJRLs covering a broad taxonomic range were used: Artocarpin from Artocarpus integrifolia (jackfruit, Moraceae), BanLec from Musa acuminata (banana, Musaceae), Calsepa from Calystegia sepium (hedge bindweed, Convolvulaceae), CCA from Castanea crenata (Japanese chestnut, Fagaceae), Conarva from Convolvulus arvensis (bindweed, Convolvulaceae), CRLL from Cycas revoluta (King Sago palm tree, Cycadaceae), Heltuba from Helianthus tuberosus (Jerusalem artichoke, Asteraceae) and MornigaM from Morus nigra (black mulberry, Moraceae). The result using 103 pyridylaminated glycans clearly divided the mJRLs into two major groups, each of which was further divided into two subgroups based on the preference for high-mannose-type N-glycans. This criterion also applied to the binding preference for complex-type N-glycans. Notably, the result of cluster analysis of the amino acid sequences clearly corresponded to the above specificity classification. Thus, marked correlation between the sugar-binding specificity of mJRLs and their phylogeny should shed light on the functional significance of JRLs.
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The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold
Journal of Biological Chemistry, 2003Co-Authors: Yves Bourne, Willy J. Peumans, Annick Barre, E J Van Damme, Véronique Roig-zamboni, Corinne Houlès Astoul, Pierre RougéAbstract:Abstract The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same β-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded β-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the β-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
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Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β‐amylase from Calystegia sepium (hedge bindweed) rhizomes
European Journal of Biochemistry, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
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purification characterization immunolocalization and structural analysis of the abundant cytoplasmic β amylase from Calystegia sepium hedge bindweed rhizomes
FEBS Journal, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
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Carbohydrate binding properties of banana (Musa acuminata) lectin: II. Binding of laminaribiose oligosaccharides and β-glucans containing β1,6-glucosyl end groups
European Journal of Biochemistry, 2001Co-Authors: Irwin J. Goldstein, Harry C. Winter, E J Van Damme, Akira Misaki, Willy J. PeumansAbstract:This paper extends our knowledge of the rather bizarre carbohydrate binding poperties of the banana lectin (Musa acuminata). Although a glucose/mannose binding protein which recognizes alpha-linked gluco-and manno-pyranosyl groups of polysaccharide chain ends, the banana lectin was shown to bind to internal 3-O-alpha-D-glucopyranosyl units. Now we report that this lectin also binds to the reducing glucosyl groups of beta-1,3-linked glucosyl oligosaccharides (e.g. laminaribiose oligomers). Additionally, banana lectin also recognizes beta1,6-linked glucosyl end groups (gentiobiosyl groups) as occur in many fungal beta1,3/1,6-linked polysaccharides. This behavior clearly distinguishes the banana lectin from other mannose/glucose binding lectins, such as concanavalin A and the pea, lentil and Calystegia sepium lectins.
Pierre Rougé - One of the best experts on this subject based on the ideXlab platform.
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The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold
Journal of Biological Chemistry, 2003Co-Authors: Yves Bourne, Willy J. Peumans, Annick Barre, E J Van Damme, Véronique Roig-zamboni, Corinne Houlès Astoul, Pierre RougéAbstract:Abstract The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same β-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded β-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the β-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
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Structure of an RNase-related protein from Calystegia sepium.
Acta Crystallographica Section D Biological Crystallography, 2002Co-Authors: Anja Rabijns, Willy J. Peumans, Christel Verboven, Pierre Rougé, Annick Barre, E. J. M. Van Damme, C. J. De RanterAbstract:The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical α + β structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the `active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
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Structure of an RNase-related protein from Calystegia sepium.
Acta crystallographica. Section D Biological crystallography, 2002Co-Authors: Anja Rabijns, Willy J. Peumans, Christel Verboven, Pierre Rougé, Annick Barre, E. J. M. Van Damme, C. J. De RanterAbstract:The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
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Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β‐amylase from Calystegia sepium (hedge bindweed) rhizomes
European Journal of Biochemistry, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
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purification characterization immunolocalization and structural analysis of the abundant cytoplasmic β amylase from Calystegia sepium hedge bindweed rhizomes
FEBS Journal, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
Annick Barre - One of the best experts on this subject based on the ideXlab platform.
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The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold
Journal of Biological Chemistry, 2003Co-Authors: Yves Bourne, Willy J. Peumans, Annick Barre, E J Van Damme, Véronique Roig-zamboni, Corinne Houlès Astoul, Pierre RougéAbstract:Abstract The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same β-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded β-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the β-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
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Structure of an RNase-related protein from Calystegia sepium.
Acta Crystallographica Section D Biological Crystallography, 2002Co-Authors: Anja Rabijns, Willy J. Peumans, Christel Verboven, Pierre Rougé, Annick Barre, E. J. M. Van Damme, C. J. De RanterAbstract:The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical α + β structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the `active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
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Structure of an RNase-related protein from Calystegia sepium.
Acta crystallographica. Section D Biological crystallography, 2002Co-Authors: Anja Rabijns, Willy J. Peumans, Christel Verboven, Pierre Rougé, Annick Barre, E. J. M. Van Damme, C. J. De RanterAbstract:The structure of a catalytically inactive RNase-related protein from Calystegia sepium (CalsepRRP) has been resolved by protein crystallography at a resolution of 2.05 A and an R factor of 20.74%. Although the protein is completely devoid of ribonuclease activity, it adopts the typical alpha + beta structure of non-base-specific RNases. Analysis of the structure revealed that two amino-acid substitutions in the 'active' P1 site, in combination with the less hydrophobic/aromatic character of the B1 base-recognition site and a completely disrupted B2 base-recognition site, might account for this complete lack of activity.
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Purification, characterization, immunolocalization and structural analysis of the abundant cytoplasmic β‐amylase from Calystegia sepium (hedge bindweed) rhizomes
European Journal of Biochemistry, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
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purification characterization immunolocalization and structural analysis of the abundant cytoplasmic β amylase from Calystegia sepium hedge bindweed rhizomes
FEBS Journal, 2001Co-Authors: E J Van Damme, Pierre Rougé, Annick Barre, Bettina Hause, Geert Baggerman, Willy J. PeumansAbstract:An abundant catalytically active β-amylase (EC 3.2.1.2) was isolated from resting rhizomes of hedge bindweed (Calystegia sepium). Biochemical analysis of the purified protein, molecular modeling, and cloning of the corresponding gene indicated that this enzyme resembles previously characterized plant β-amylases with regard to its amino-acid sequence, molecular structure and catalytic activities. Immunolocalization demonstrated that the β-amylase is exclusively located in the cytoplasm. It is suggested that the hedge bindweed rhizome β-amylase is a cytoplasmic vegetative storage protein.
E. Schlösser - One of the best experts on this subject based on the ideXlab platform.
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Weeds as alternative hosts for BSBV, BNYVV, and the vector Polymyxa betae (German isolate)
Journal of Plant Diseases and Protection, 2008Co-Authors: A. M. Mouhanna, Gregor Langen, E. SchlösserAbstract:When grown in contaminated soil, several weed species proved to be alternative hosts for the Beet necrotic yellow vein virus (BNYVV), the Beet soil-borne virus (BSBV), and their common vector Polymyxa betae . The monocotyledonous plants Alopecurus myosuroides, Lolium multiflorum, Sorghum vulgare, Sorghum halepense and dicotyledonous plants Calystegia sepium, Capsella bursa-pastoris, Centaurea cyanus, Convolvulus arvensis, Galinsorga parviflora, Matricaria inodora, Stellaria media were positively tested, whereas Chenopodium album was shown to be a host for P. betae , but couldn’t be verified in ELISA to be a host for the viruses. The status of the weeds as alternative hosts was confirmed by positive re-transmission of the viruses by their vector from infected weed roots to susceptible sugar beet plants. ITS sequence and northern blot analysis proved P. betae but not P. graminis to be the vector for the virus transmission from weeds. Verschiedene Wildkrautarten erwiesen sich als alternative Wirte für BNYVV, BSBV und ihren gemeinsamen Vektor Polymyxa betae , wenn sie in kontaminierter Erde wuchsen. Die monokotyledonen Pflanzen Alopecurus myosuroides, Lolium multiflorum, Sorghum vulgare, Sorghum halepense und die Dikotyledonen Calystegia sepium, Capsella bursa-pastoris, Centaurea cyanus, Convolvulus arvensis, Galinsorga parviflora, Matricaria inodora, Stellaria media wurden positiv getestet, wohingegen Chenopodium album sich zwar als Wirt für P. betae erwies, jedoch konnten im ELISA die zwei Viren nicht zweifelsfrei nachgewiesen werden. Der Status der Wildkräuter als alternative Wirtspflanzen wurde durch eine positive Retransmission der Viren durch ihren Vektor von infizierten Wildkrautwurzeln auf anfällige Zuckerrübenpflanzen bestätigt. ITS-Sequenzanalysen und Northern-Blot-Analysen bewiesen, dass P. betae , nicht jedoch P. graminis der Vektor für die Virustransmission von Wildkräutern war.
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Weeds as alternative hosts for BSBV, BNYVV, and the vector Polymyxa betae (German isolate)
Journal of Plant Diseases and Protection, 2008Co-Authors: A. M. Mouhanna, Gregor Langen, E. SchlösserAbstract:When grown in contaminated soil, several weed species proved to be alternative hosts for the Beet necrotic yellow vein virus (BNYVV), the Beet soil-borne virus (BSBV), and their common vector Polymyxa betae. The monocotyledonous plants Alopecurus myosuroides, Lolium multiflorum, Sorghum vulgare, Sorghum halepense and dicotyledonous plants Calystegia sepium, Capsella bursa-pastoris, Centaurea cyanus, Convolvulus arvensis, Galinsorga parviflora, Matricaria inodora, Stellaria media were positively tested, whereas Chenopodium album was shown to be a host for P. betae, but couldn’t be verified in ELISA to be a host for the viruses. The status of the weeds as alternative hosts was confirmed by positive re-transmission of the viruses by their vector from infected weed roots to susceptible sugar beet plants. ITS sequence and northern blot analysis proved P. betae but not P. graminis to be the vector for the virus transmission from weeds.
